Inactivation of PEMT2 in hepatocytes initiated by DENA in fasted/refed rats
- Giannina Gaslini Institute, Genova (Italy)
- DISCAFF Department, University 'Amedeo Avogadro', Novara (Italy)
- Department of Biotecnological and Biomolecular Sciences, University of Milan, Milan (Italy)
- Department of Experimental Medicine, General Pathology Section, University of Genoa, Genoa (Italy)
Phosphatidylethanolamine N-methyltransferase (PEMT) is the enzyme that converts phosphatidylethanolamine (PE) into phosphatidylcholine. We have previously shown that PEMT suppressed hepatoma growth by triggering apoptosis. We investigate whether PEMT controlled cell death and cell proliferation triggered by fasting/refeeding and whether it is a marker of early preneoplastic lesions. The induction of programmed cell death and suppression of cell proliferation by fasting were associated with enhanced PEMT expression and activity, and with a decrease in CTP:phosphocholine cytidylyltransferase expression. Refeeding returned the liver growth and expression of CTP:phosphocholine cytidylyltransferase to control levels, while the expression of PEMT decreased to below control values. After DENA administration, PEMT protein, evaluated by Western blotting, slightly increased, but it remained below control levels. The treatment with 20 mg/kg DENA to refed rats induced the appearance of initiated hepatocytes that were negative for PEMT expression. Present findings indicate that PEMT is a novel tumour marker for early liver preneoplastic lesions.
- OSTI ID:
- 20854370
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 346, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2006.05.101; PII: S0006-291X(06)01168-5; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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